%0 Journal Article %1 citeulike:514407 %A Clifton, I. J. %A Hsueh, L. C. %A Baldwin, J. E. %A Harlos, K. %A Schofield, C. J. %C The Dyson Perrins Laboratory and the Oxford Centre for Molecular Sciences, Oxford, UK. %D 2001 %J Eur J Biochem %K oxoglutarate oxygenases iron %N 24 %P 6625--6636 %T Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases. %U http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=pubmed&dopt=Abstract&list_uids=11737217 %V 268 %X Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyse oxidative reactions in a range of metabolic processes including the hydroxylation of proline and lysine residues during the post-translational modification of collagen. 2-OG oxygenases commonly require ascorbate for full activity. In the vitamin C deficient disease, scurvy, reduced activity of 2-OG oxygenases results in impaired formation of collagen. Here we report the crystal structure of bacterial proline 3-hydroxylase from Streptomyces sp., an enzyme which hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. Structures were obtained for the enzyme in the absence of iron (to 2.3A resolution, R=20.2%, Rfree=25.3%) and that complexed to iron (II) (to 2.4A resolution, R=19.8%, Rfree=22.6%). The structure contains conserved motifs present in other 2-OG oxygenases including a 'jelly roll' beta strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. The structure differs significantly from many other 2-OG oxygenases in possessing a discrete C-terminal helical domain. Analysis of the structure suggests a model for proline binding and a mechanism for uncoupling of proline and 2-OG turnover.

@article{citeulike:514407, abstract = {Iron (II)/2-oxoglutarate (2-OG)-dependent oxygenases catalyse oxidative reactions in a range of metabolic processes including the hydroxylation of proline and lysine residues during the post-translational modification of collagen. 2-OG oxygenases commonly require ascorbate for full activity. In the vitamin C deficient disease, scurvy, reduced activity of 2-OG oxygenases results in impaired formation of collagen. Here we report the crystal structure of bacterial proline 3-hydroxylase from Streptomyces sp., an enzyme which hydroxylates proline at position 3, the first of a 2-OG oxygenase catalysing oxidation of a free alpha-amino acid. Structures were obtained for the enzyme in the absence of iron (to 2.3A resolution, R=20.2%, Rfree=25.3%) and that complexed to iron (II) (to 2.4A resolution, R=19.8%, Rfree=22.6%). The structure contains conserved motifs present in other 2-OG oxygenases including a 'jelly roll' beta strand core and residues binding iron and 2-oxoglutarate, consistent with divergent evolution within the extended family. The structure differs significantly from many other 2-OG oxygenases in possessing a discrete C-terminal helical domain. Analysis of the structure suggests a model for proline binding and a mechanism for uncoupling of proline and 2-OG turnover.}, added-at = {2007-02-02T11:54:15.000+0100}, address = {The Dyson Perrins Laboratory and the Oxford Centre for Molecular Sciences, Oxford, UK.}, author = {Clifton, I. J. and Hsueh, L. C. and Baldwin, J. E. and Harlos, K. and Schofield, C. J.}, biburl = {https://www.bibsonomy.org/bibtex/2d2fea5d76ad357f147453e6163e0d5d5/robert}, citeulike-article-id = {514407}, interhash = {fba0f4618723991c11ff5e1e88d17694}, intrahash = {d2fea5d76ad357f147453e6163e0d5d5}, issn = {0014-2956}, journal = {Eur J Biochem}, keywords = {oxoglutarate oxygenases iron}, month = {December}, number = 24, pages = {6625--6636}, priority = {2}, timestamp = {2007-02-02T11:54:15.000+0100}, title = {Structure of proline 3-hydroxylase. Evolution of the family of 2-oxoglutarate dependent oxygenases.}, url = {http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve\&db=pubmed\&dopt=Abstract\&list_uids=11737217}, volume = 268, year = 2001 }